1.7.3.3: factor-independent urate hydroxylase
This is an abbreviated version!
For detailed information about factor-independent urate hydroxylase, go to the full flat file.
Word Map on EC 1.7.3.3
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1.7.3.3
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hyperuricemia
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peroxisomal
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xanthine
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allopurinol
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gout
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purine
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catalase
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allantoin
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biosensors
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electrode
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hematologic
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creatinine
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oxonic
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febuxostat
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allantoinase
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hyperkalemia
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hypoxanthine
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prophylaxis
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flavus
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hyperphosphatemia
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urate-lowering
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ureide
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methemoglobinemia
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pegylated
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amperometric
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uricosuric
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hypocalcemia
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tophi
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benzbromarone
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hominoid
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phosphotungstate
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microbodies
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hypouricemic
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probenecid
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utilis
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pimecrolimus
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pharmacology
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medicine
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analysis
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synthesis
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weight-based
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nodule-specific
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miocene
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drug development
- 1.7.3.3
- hyperuricemia
- peroxisomal
- xanthine
- allopurinol
- gout
- purine
- catalase
- allantoin
-
biosensors
-
electrode
-
hematologic
- creatinine
-
oxonic
- febuxostat
- allantoinase
- hyperkalemia
- hypoxanthine
-
prophylaxis
- flavus
- hyperphosphatemia
-
urate-lowering
-
ureide
- methemoglobinemia
-
pegylated
-
amperometric
-
uricosuric
-
hypocalcemia
-
tophi
- benzbromarone
-
hominoid
-
phosphotungstate
- microbodies
-
hypouricemic
- probenecid
- utilis
- pimecrolimus
- pharmacology
- medicine
- analysis
- synthesis
-
weight-based
-
nodule-specific
-
miocene
- drug development
Reaction
Synonyms
AaUO, AgUOX, dHU-wPU, ELITEK, Fasturtec, MVSM, N-35, Nodule specific uricase, Nodulin 35, Nodulin 35 homolog, Non-symbiotic uricase, oxidase, urate, Pucl, Rasburicase, Uaz, Uox, Urate oxidase, urate oxidoreductase, UriA, uric acid oxidase, uricase, uricase II, Uricoenzyme, Uricozyme
ECTree
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Engineering
Engineering on EC 1.7.3.3 - factor-independent urate hydroxylase
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K12C/E286C
the mutations introduce disulfide bonds between the subunits and markedly increase the melting temperature (from 61 to 75°C) of the enzyme compared with wild type
S296C/C302S
the mutations introduce disulfide bonds between the subunits and markedly increase the melting temperature (from 61 to 70°C) of the enzyme compared with wild type
K9M
T69A
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mutant enzyme has a maximal velocity of 3% of the wild-type value. Ionization at pH 6.4 that is observed with the wild-type enzyme is absent in the mutant. The KM-value for urate is 5fold higher than that of the wild-type enzyme
T69A/K9M
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the KM-value for urate is 16.1fold higher than that of the wild-type enzyme
T69V
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the KM-value for urate is 30.9fold higher than that of the wild-type enzyme
C249S
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the substitution has no effect on enzymatic activity
C249S/DELTAL302
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the combination of both mutations increases the enzymatic activity by 8%.Tthe specific activity of the mutant enzyme does not decrease after exposed to 37°C for 20 h
DELTAL302
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the mutant has improved specific activity (6%) compared with wild type enzyme
A89T/G91A7V92M/H245L/E252A/M253I/R291K/A296V/A301S/K303R
replacement with the corresponding residues of human enzyme. About 30% of wild-type catalytic efficiency
H245L/E252A/M253I/R291K/A296V/A301S/K303R
replacement with the corresponding residues of human enzyme. Catalytic efficiency is higher than in wild-type, but below the efficiency of mutant R291K/A296V/A301S/K303R
I115V/H119R/L120F/H245L/E252A/M253I/R291K/A296V/A301S/K303R
replacement with the corresponding residues of human enzyme, complete loss of activity
R291K/A296V/A301S/K303R
replacement with the corresponding residues of human enzyme. About 50% increase in catalytic efficiency
A132C/A225C
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
D288C
the mutant shows 0.8fold reduced catalytic efficiency compared to the wild type enzyme
I27C/N289C
the mutant with 0.45fold reduced catalytic efficiency has similar specific activity and production yield to that of wild type but its thermostability is dramatically improved (120fold increase in half-life at 37°C)
N289C
the mutant 0.3fold reduced catalytic efficiency compared to the wild type enzyme
S136C
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
L171I/Y182F/Y187F/A193S
mutant displays higher activity and lower thermostability
L322R
mutant shows reduced activity and thermal stability at pH 7.4, enhanced stability at pH 9.2
R310E
displays the lowest stability at pH 7.4 or 9.2 among tested mutants and the strongest effects of pH values on thermal stability
S314Stop
mutant is a homotetramer of about 25% activity, 5 % half-life at pH 7.4 but 100 % half-life at pH 9.2
V144A
V144A/Y319R
Y249F
thermal stability is reduced by 50fold at pH 7.4, by about 7fold at pH 9.2
Y319F
thermal stability is reduced by one magnitude at pH 7.4, but by 2fold at pH 9.2
Y319R
the mutant shows wild type activity and has much stronger thermostability than the wild type enzyme
D307R
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mutant is an inactive homotetramer of lower solubility
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R310E
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displays the lowest stability at pH 7.4 or 9.2 among tested mutants and the strongest effects of pH values on thermal stability
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Y249F
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thermal stability is reduced by 50fold at pH 7.4, by about 7fold at pH 9.2
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Y319F
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thermal stability is reduced by one magnitude at pH 7.4, but by 2fold at pH 9.2
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synthesis
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expression of baboon uricase gene attached with Trx and hexahistidine tags in Escherichia coli Rosetta (DE3). The final yield of mature baboon uricase is 136.0 mg/l with enzyme activity of 17.93 U/mg
additional information
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mutant enzyme has a maximal velocity of 0.4% of the wild-type value. Ionization at pH 6.4 that is observed with the wild-type enzyme is absent in the mutant. The KM-value for urate is 1.5fold higher than that of the wild-type enzyme
K9M
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mutant is not able to generate the dianion of urate and is decreased in activity by over 200-fold
mutant displays higher activity and consistent thermostability
V144A
the mutant has about 25% increase of the activity against wild type
the mutant has about 25% increase of the activity against wild type
V144A/Y319R
the mutant shows an approximately 4 week lagging phase before the exponential activity decrease, an apparent half-life of activity nearly 3folds of mutant V144A, but comparable activity
additional information
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uricase covalently linked to monomethoxypoly(ethylene glycol) N-leucine-OSu, branched monomethoxypoly(ethylene glycol) N-leucine-OSu or poly(N-acryloylmorpholine)-OSu last longer in blood
additional information
the folding of the C-terminal residues is crucial for thermal stability. When positive charge on residue R3 is eliminated, the mutants become inactive dimers
additional information
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the folding of the C-terminal residues is crucial for thermal stability. When positive charge on residue R3 is eliminated, the mutants become inactive dimers
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additional information
the recombinantly expressed porcine enzyme, with a C-terminal sequence from baboon uricase, is applicated to patients with refractory gout, due to a mutation in the uricase gene, by intravenous injection in a PEG-bound form, pharmacokinetics and pharmacodynamics, safety, and efficacy of the treatment in a clinical trial, overview